ID A0A162YPP1_DIDRA Unreviewed; 1583 AA.
AC A0A162YPP1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=ATP binding {ECO:0000313|EMBL:KZM20154.1};
DE SubName: Full=Myosin type-2 heavy chain 1 {ECO:0000313|EMBL:UPX12216.1};
GN ORFNames=EKO05_0002778 {ECO:0000313|EMBL:UPX12216.1}, ST47_g8718
GN {ECO:0000313|EMBL:KZM20154.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM20154.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM20154.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM20154.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
RN [2] {ECO:0000313|EMBL:UPX12216.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX12216.1};
RX PubMed=32345704; DOI=10.1534/g3.120.401265;
RA Shah R.M., Williams A.H., Hane J.K., Lawrence J.A., Farfan-Caceres L.M.,
RA Debler J.W., Oliver R.P., Lee R.C.;
RT "Reference Genome Assembly for Australian Ascochyta rabiei Isolate
RT ArME14.";
RL G3 (Bethesda) 10:2131-2140(2020).
RN [3] {ECO:0000313|EMBL:UPX12216.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Me14 {ECO:0000313|EMBL:UPX12216.1};
RA Mobegi F.M., Debler J.W.D., Lee R.C.L.;
RL Submitted (MAR-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYNV01000285; KZM20154.1; -; Genomic_DNA.
DR EMBL; CP095291; UPX12216.1; -; Genomic_DNA.
DR STRING; 5454.A0A162YPP1; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR Proteomes; UP000617380; Chromosome 4.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd15480; fMyo2p_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.10.287.1490; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR046943; Fungal_Myo2/2A_CBD.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140:SF860; DILUTE CLASS UNCONVENTIONAL MYOSIN, ISOFORM C; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 3.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF50084; Myosin S1 fragment, N-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 6..61
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 74..780
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1224..1493
FT /note="Dilute"
FT /evidence="ECO:0000259|PROSITE:PS51126"
FT REGION 655..677
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1038..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1554..1583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1056
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 168..175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1583 AA; 180177 MW; 88193D4B692F8419 CRC64;
MAHIYDIGTR AWQPDTTEGW VASEVADKQI DGDKVKLLFQ LENGETKTVE TTLLAIQTGN
DPNLPPLMNP AMLEASDDLT NLSHLNEPAV LQAIKLRYLQ NEIYTYSGIV LIATNPFARV
DSLYVPGMVQ VYAGKQRSYG APHLFAIAEE AFADMLRDQK NQTIVVSGES GAGKTVSAKY
IMRYFATRES PDNPGKRRGK IDSMSETEEQ ILATNPIMEA FGNAKTTRND NSSRFGKYIE
IMFNKQTDII GAKIRTYLLE RSRLVFQPLK ERNYHIFYQL VAGATDAERE ELSLKPVEDF
SYLNQGSAPI IDGMDDKAEF EATKSSLTKI GVPQATQAQI FRLLAALLHM GDVKITATRT
DSNLAPDEPA LVKACGLLGI DANNFAKWTV KKQLITRGEK IVSNLTQQQA VVVRDSVAKF
IYSSLFDWLV ERTNESLATE EVITHAHSFI GVLDIYGFEH FAKNSFEQFC INYANEKLQQ
EFNAHVFKLE QEEYMREQID WTFIDFADNQ PCIDLIEGKL GILSLLDEES RLPMGSDEQF
VTKLHHNYSG DKHKFYKKPR FGKSAFTVCH YAVDVTYESD GFIEKNRDTV PDEHMEVLKA
SSNKFLAEVL DVASQIREKE TAASTSAKAG TTMSAGRRMA TNRKPTLGGI FKSSLIELMS
TINSTDVHYI RCIKPNEAKA AWQFDGPMVL SQLRACGVLE TVRISCAGYP TRWTYEEFAL
RYYMLVQSSG WTPEIRDMAK AILHKALGNS KNDGTDKYQM GLTKIFFRAG MLAFLENLRT
ARLNDAAIMI QKNLRAKYYR RIYLEMRQAI VAVQSLARGY MTRGRAEEAR QVKAATTIQR
VWRGSKDRKR FHLVRRSVIL FQAAAKGFLC RKNILDTRLG NAARIIQRTW RSQRSLKAWR
QYRKKIVTIQ KLWRGKTARK EYKVLRAESR DLKNISYKLE NKVVELTQTL GSMKEQNKSL
KQQVDNYENQ IKSYKERSRA LENRQKELQV EANQAGITAA KLSQMEDEFK KLQTNYDEST
AKMRHLQEEE KQLRASLKQT TDELDNSRRR SNVTETEKTS LRQQLADLQE QVELMKRSGP
IHSTLENGST PIAASSLINL VSSKKPKRRS AGPDTRDLDR FSATYNPRPV SMAVGSTVHR
QNLSGSTFAQ LDNVELELEN ILADEDMLND EVTLGLIKNL KIPSPTTTPP PTDKEVLFPA
YLINLVTSEM WNNGFVKESE RFLANVMQSI QQEVMQHDSD DAINPGAFWL SNVHEMLSFV
FLAEDWYEQQ KTDNYEYDRL LEIVKHDLES LEFNIYHTWM KVLKKKLHKM IIPAIIESQS
LPGFVTNESN RFLGKLLQGS NTPAYSMDNL LSLLNSVYKA MKAFYLEDTI ITQCVTELLR
LVGVTAFNDL LMRRNFLSWK RGLQINYNIT RIEEWCKSHD MPEGTLQLEH LMQATKLLQL
KKATLNDIEI IQDICWMLSP NQIQKLLNQY LIADYEQPIN GEIMKAVASR VTEKSDVLLL
TAVDMEDSGP YEIAEPRVIT ALETYTPSWL QTPRLKRLAE IVSQQAIAQQ EKMEFDGPSP
NENGNGANGF HNGHESIMEE VGA
//